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2HDN

Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]298
Detector technologyAREA DETECTOR
DetectorSDMS
Spacegroup nameP 1 21 1
Unit cell lengths69.710, 156.060, 134.830
Unit cell angles90.00, 95.38, 90.00
Refinement procedure
Resolution40.000 - 2.800
Rwork0.180
R-free0.22300
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)an unrefined 2.7 Angstrom model of E. coli trypsin-modified EF-Tu-MgGDP consisting of residues 9 to 40 50 to 258 and 260 to 393 plus one Mg ion and GDP
RMSD bond length0.020
RMSD bond angle1.820
Phasing softwareMERLOT
Refinement softwareCNS
Data quality characteristics
 Overall
Low resolution limit [Å]47.300
High resolution limit [Å]2.700
Rmerge0.099
Number of reflections73085
Completeness [%]92.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROPMultiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP

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PDB entries from 2024-07-10

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